ID A0A352X952_9CYAN Unreviewed; 556 AA. AC A0A352X952; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 25-MAY-2022, entry version 13. DE RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000256|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01283}; DE Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_01283}; DE EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_01283}; DE EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_01283}; DE AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_01283}; GN Name=ribBA {ECO:0000256|HAMAP-Rule:MF_01283}; GN ORFNames=DDW51_13290 {ECO:0000313|EMBL:HBE18551.1}; OS Cyanobacteria bacterium UBA11367. OC Bacteria; Cyanobacteria. OX NCBI_TaxID=2055774 {ECO:0000313|EMBL:HBE18551.1, ECO:0000313|Proteomes:UP000263299}; RN [1] {ECO:0000313|EMBL:HBE18551.1, ECO:0000313|Proteomes:UP000263299} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA11367 {ECO:0000313|EMBL:HBE18551.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate CC and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000256|ARBA:ARBA00002284, ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6- CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and CC pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + CC formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830; CC EC=4.1.99.12; Evidence={ECO:0000256|ARBA:ARBA00000141, CC ECO:0000256|HAMAP-Rule:MF_01283}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)- CC pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25; CC Evidence={ECO:0000256|ARBA:ARBA00029293, ECO:0000256|HAMAP- CC Rule:MF_01283}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000256|HAMAP-Rule:MF_01283}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01283}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3- CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. CC {ECO:0000256|ARBA:ARBA00004904, ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D- CC ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|ARBA:ARBA00004853, CC ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase CC family. {ECO:0000256|ARBA:ARBA00005520, ECO:0000256|HAMAP- CC Rule:MF_01283}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HBE18551.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DNOY01000287; HBE18551.1; -; Genomic_DNA. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000263299; Unassembled WGS sequence. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00641; GTP_cyclohydro2; 1. DR Gene3D; 3.40.50.10990; -; 1. DR HAMAP; MF_00179; RibA; 1. DR HAMAP; MF_00180; RibB; 1. DR HAMAP; MF_01283; RibBA; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR InterPro; IPR032677; GTP_cyclohydro_II. DR InterPro; IPR000926; RibA. DR InterPro; IPR036144; RibA-like_sf. DR InterPro; IPR016299; Riboflavin_synth_RibBA. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF142695; SSF142695; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00505; ribA; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 3: Inferred from homology; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_01283}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01283}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000313|EMBL:HBE18551.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01283}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01283}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01283}; Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01283}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_01283}; Zinc {ECO:0000256|HAMAP-Rule:MF_01283}. FT DOMAIN 221..385 FT /note="GTP_cyclohydro2" FT /evidence="ECO:0000259|Pfam:PF00925" FT NP_BIND 264..268 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT NP_BIND 307..309 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 1..211 FT /note="DHBP synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 35..36 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 150..154 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 212..556 FT /note="GTP cyclohydrolase II" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 341 FT /note="Proton acceptor; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 343 FT /note="Nucleophile; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 36 FT /note="Magnesium or manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 36 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 153 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 269 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 280 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 282 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 40 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 174 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 285 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 329 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 364 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 369 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 136 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 174 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" SQ SEQUENCE 556 AA; 61819 MW; 068AA2C1E0005EE3 CRC64; MESSETNLFE FDSIDAALED LKAGRALVVV DDENRENEGD LICAAQFATP DMINFMAVEA RGLICLALTG QRLDELDVPL MVSKNTDSNQ TAFTISIDAS THVGVTTGIS AEDRAKTIQV AIDPHTKPSD LRRPGHIFPI RAKEGGVLKR AGHTEAAVDL PRLAGLYPAG VICEIQNLDG SMARLPQLVK YAKYHQLKLI SIADLIGYRL KYDRFVYRES VAKLPSVFGN FEIYGYRNAL DNSEHVAIVK GNPAEFQDNP VMVRMHSECL TGDGLGSLRC DCRMQLEAAL KMIENAGQGV VVYLRQEGRG IGLVNKLKAY SLQDMGLDTV EANERLGFPA DLRDYGMGAQ MLNDIGVQKI RLITNNPRKI AGLRGYGLEV VDRVPLLIES NDYNSTYLAT KAQKLGHLLL QTYLVSVAIH WNDAPEGIEQ RYERLEKIRS LVHSQNLLLQ EESRPVAIAL FDKPSLIVHL GFDQANLAAP DWYKNTQHPY LQAILKILDT LSQWPQVGRL AILISSGIDP LTSLQVRLDR ERLPLTQPPS LICDRLSTQK VYSFDR //